Denaturant-induced expansion and compaction of a multi-domain protein: IgG. - Wikidata - wikimedia - TriplyDB

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

http://www.wikidata.org/entity/Q37040767

about

Unfolded-state dynamics and structure of protein L characterized by simulation and experiment Spectroscopic studies of protein folding: linear and nonlinear methods Heterogeneous diffusion of a membrane-bound pHLIP peptide.Photoinduced electron transfer and fluorophore motion as a probe of the conformational dynamics of membrane proteins: application to the influenza a M2 proton channel Simple method to enhance the photostability of the fluorescence reporter R6G for prolonged single-molecule studies.Slow and bimolecular folding of a de novo designed monomeric protein DS119.How force unfolding differs from chemical denaturation.Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Diffusion as a probe of the heterogeneity of antimicrobial peptide-membrane interactions.Guanidinium-Induced Denaturation by Breaking of Salt Bridges.E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form

P2860

Q24596398-49D63CA7-5504-468C-AF3F-4DD03F032996 Q31042100-0BB41824-ED5D-49C8-9AE9-CFCAD1A67922 Q33908287-5791CDE8-0F39-4335-B5DF-BAC4FD06EC99 Q34744629-751FA373-0493-4D13-BCE2-BAEC6AE70BA6 Q37045949-C4DA7571-7AAC-4A11-9F0C-8CAC826201E6 Q37299575-ABDFDE7E-474F-46B5-AF56-8D348A973F6A Q37628029-D9CE2F69-F5A9-4A3A-9051-17FE6DDBA1A6 Q39432831-D3111846-2CE8-4EB9-AD17-9E59E3D6A0B1 Q40900833-92E90ACB-6912-4386-9FBF-497E25845CBE Q52664708-A2098559-A6C0-44CF-B63F-3808B5C8646A Q58788156-4B49AF5A-392B-4B4A-B1D0-D1FE52AE9973

P2860

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

http://www.wikidata.org/entity/Q37040767

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 18 March 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

@en

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

@nl

type

label

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

@en

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

@nl

prefLabel

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

@en

Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

@nl

P1433

Q37040767-8C33A1C9-B97E-44A5-9872-51E201C43088

P1476

Q37040767-74D0ED91-60E8-4860-8D25-1EFA4518C5BA

P2093

Q37040767-1DD127E7-02FF-4405-9EB9-3DACED539F85

Q37040767-85C37E91-2249-4DFD-9B6C-31D39B91414A

Q37040767-948683FF-77FA-4F58-B990-812DA0C640FC

P2860

Q37040767-0123415F-F1D5-455D-A59F-795FAF7060E6

Q37040767-01A56319-A2D0-4D0A-A5F7-9BC85CF38BD5

Q37040767-0538E358-19E5-4B24-878C-314163D36DE3

Q37040767-0CFDFE64-46FF-41CA-A5DF-F737C9AAADC6

Q37040767-0FE7ACE9-2EB2-4B6A-9CAB-9646DFD4F6C9

Q37040767-1CA64C12-AA13-4DD2-BDFF-B57BAEB5D851

Q37040767-213BE8B5-86BD-4C57-9DA0-4AC097A73B0E

Q37040767-31A68464-CA25-4349-B20E-38663A852E1D

Q37040767-38012DAF-17CF-4B20-9D9C-C3FBC08155FC

Q37040767-3D43784E-5A55-4282-AD82-D90BB2C14C4C

P304

Q37040767-93E5F749-ED3B-49FE-AA61-B90941B43DE5

P31

Q37040767-5997B15E-E4B3-481E-93E4-E556E49E5098

P356

Q37040767-DB0119A7-9B19-4409-8BB9-6F9A9221189D

P407

Q37040767-FD298F08-8095-433B-9666-5B1D470DCD08

P433

Q37040767-C1A67711-0BBB-4CCB-B3A5-637688FF0CDE

P478

Q37040767-AB2B581E-DC5D-44C4-A954-C874683CEC81

P50

Q37040767-FE4BDD7E-57AD-4F2A-BAC1-CCD5B46332E9

P577

Q37040767-A188AC5A-15A9-404C-AE53-53163B453AA3

P5875

Q37040767-A4517A37-3885-463F-85F5-247CA8FB26C8

P698

Q37040767-35ED101E-D5A3-4ED3-838D-1FE168887DA9

P932

Q37040767-BFDC8FB8-90CD-4DD7-BC4C-28F94195CF3D

P356

J.JMB.2008.03.006

P1433

Journal of Molecular Biology

P1476

Denaturant-induced expansion and compaction of a multi-domain protein: IgG

@en

P2093

Feng Gai

http://www.w3.org/2001/XMLSchema#string

Julie M Glasscock

http://www.w3.org/2001/XMLSchema#string

Lin Guo

http://www.w3.org/2001/XMLSchema#string

P2860

The immunoglobulin fold. Structural classification, sequence patterns and common core

Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques.

Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding.

Statistical coil model of the unfolded state: resolving the reconciliation problem.

Fluorescence correlation spectroscopy: novel variations of an established technique.

A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins

Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions.

A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.

Resolution of fluorescence correlation measurements

P304

1029-1036

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.JMB.2008.03.006

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

384

http://www.w3.org/2001/XMLSchema#string

P50

Pramit Kumar Chowdhury

P577

2008-03-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

23468899

http://www.w3.org/2001/XMLSchema#string

P698

19004457

http://www.w3.org/2001/XMLSchema#string

P932

2615248

http://www.w3.org/2001/XMLSchema#string